Winarto Haryadi

Thin‐layer chromatography and gas chromatography–mass spectrometry examination of shoe materials from patients with shoe dermatitis

Keywords: 2(3H)-benzothiazolone; 7-oxodehydroabietic acid methyl ester; colophonium; contact dermatitis; gas chromatography–mass spectrometry (GCMS); methyl dehydroabietate; patch testing; shoes; thin-layer chromatography (TLC)

Partial purification and biochemical characterization of extracellular lipase from Azospirillum sp. JG3 bacteria

An extracellular lipase from Azospirillum sp.JG3 bacteria was partially purified by ammonium sulfate fractionation. Production of crude extract lipase in Nutrient Broth medium fortified with 1 % olive oil as inducer, fractionation of lipase using ammonium sulfate, and characterization of the highest specific activity of lipase fraction have been achieved in this study. The ammonium sulfate lipase fraction which has highest specific activity is F60 with its value is 12,283.33 U/mg protein. The optimum lipase activity of F60 was achieved at 40° C and pH 7.0. The addition of 1.0 mM EDTA strongly decreased its activity. It considered that this lipase was a metalloenzyme. The addition of 1.0 mM Ca2+ solution showed that this metal ion increased lipase activity, it indicated that Ca2+ ion is an activator of this lipase. Whereas addition of Mg2+, Zn2+, Co2+, and Cu2+ metal ions decreased its activity. Effect of surfactants and commercial detergents addition towards lipase activity showed that all treatments decr...

Synthesis, in vitro and Molecular Docking Studies of 1-(3,4-Dimethoxy-phenyl)-5-(4-hydroxy-3-methoxy-phenyl)-penta-1,4-dien-3-one as New Potential Anti-inflammatory

Inflammation is a localized physical condition with heat, swelling, redness and usually pain. It is mediated by the release of proinflammatory mediators (bradykinin and cytokines), which in turn increases the rate of prostaglandin synthesis [1,2]. Nonsteroidal anti-inflammatory drugs (NSAIDs) inhibit the biosynthesis of prostaglandins by inhibiting cyclooxygenases (COXs). It exists in two isoforms i.e., a constitutive form (COX-1) and an inducible form (COX-2) [3,4]. COX-1 enzyme is responsible for maintenance of gastric integrity and kidney function [5-7] whereas COX-2 is involved in the inflammation and pain [8,9]. All classical NSAIDs, such as aspirin and indomethacin are non selective inhibitors for both COX-1 and COX-2, but bind more tightly to COX-1. In order to prevent or decrease these side effects, a current strategy consists of designing selective COX-2 inhibitors with an improved gastric safety profile [10,11]. Curcuminoids exhibited many interesting biological activities [12], for example, antioxidant activity [13,14], antiinflammatory activity [15,16], anticancer activity [13,17,18], antiprotozoal activity [19] and anti-HIV activity [20]. On the other hand, curcumin analogue such as modification of the dienone functional group curcumin into monoketone and side chain of aromatic ring with symmetrical or asymmetrical substituents possessed structural features which conferred potential biological activity and pharmaceutical use [21,22]. Synthesis, in vitro and Molecular Docking Studies of 1-(3,4-Dimethoxy-phenyl)-5-(4-hydroxy3-methoxy-phenyl)-penta-1,4-dien-3-one as New Potential Anti-inflammatory

Novel synthesis of substituted benzylidenecyclohexanone by microwave assisted organic synthesis

Benzylidenecyclohexanone derivatives are compounds with wide bioactivity. Usually, it was synthesized from cyclohexanones and benzaldehyde derivatives under base condition. This research presents a rapid and simple method to synthesis substituted benzylidenecyclohexanone. Cyclohexanone was mixed with 4-hydroxybenzaldehyde in acid condition under MAOS for 2 minutes, then it was left to cooled. Brownish purple powder in 81.47% yield was obtained. The product was identified by gas chromatography, then followed by structure elucidation by using NMR spectrophotometer. The novel compound is confirmed as 4-((E)-((1E,3’E)-3’-(4-hydroxybenzylidene)-2’-oxo-[1,1’-bi(cyclohexylidene)]-2,5-dienylidene-4-ylidene) me-thoxy)benzaldehyde.

Synthesis of Curcumin Analogues Monoketone from Cinnamaldehyde and their Inhibition Assay against Alpha-Glucosidase Enzyme

The synthesis of curcumin analogues monoketone as target compounds from cinnamaldehyde and inhibition assay against alpha-glucosidase enzyme had been performed. The stepwise of synthesis was performed by aldol condensation Claisen-Schmidt reaction andused ketones variation to give curcumin analogues monoketone. The antidiabetic activity of curcumin analogues was carried out by inhibition test against alpha-glucosidase enzyme isolated from rotten rice (Oryza sativa). The first step of synthesis was started by reacting cinnamaldehyde and monoketones such as acetone (curcumin analog A [(1E,3E,6E,8E)-1,9-diphenyl-1,3,6,8-nanotetraen-5-one]), cyclopentanone (curcumin analog B [(2E,5E)-2,5-bis ((E)-3-phenylallylidene) cyclopentanone], and cyclohexanone (curcumin analog C [(2E,6E)-2,6-bis [(E)-3-phenylallylidene] cyclohexanone]) in ethanol as solvent. The synthesis was carried out in base condition (KOH) by stirring at 52 °C for 50 minutes. The structures of all products were identified by using FTIR, direct inlet-MS, 1H-and 13C-NMR. Futhermore, the activity of curcumin analogues was tested against with alpha-glucosidase enzyme inhibition. The results show that the curcumin analogues (A-C) were yielded in 85.57; 72.15; and 82.97%, respectively as yellow solid. The melting point of curcuminanalogues (A-C) were at 116.60-122.40; 196.20-200.10; and 142.30-148.10 °C, respectively. The inhibition of alpha-glucosidase enzyme indicated that the curcumin analog B was potential to inhibit alpha-glucosidase enzyme with the highest activity by giving inhibition percentage of about 70.71% at 2.5 mM.

Molecular docking analysis of curcumin analogues with COX-2

Curcumin analogues were evaluated for COX-2 inhibitory as anti-inflammatory activities. The designed analogues significantly enhance COX-2 selectivity. The three compounds could dock into the active site of COX-2 successfully. The binding energies of -8.2, - 7.6 and -7.5 kcal/mol were obtained for three analogues of curcumin respectively. Molecular docking study revealed the binding orientations of curcumin analogues in the active sites of COX-2 towards the design of potent inhibitors.